P19211 (IF5A2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 5A-2
Short name=eIF-5A-2

Alternative name(s):
Anaerobically induced protein 1
Hypusine-containing protein HP1
eIF-4D

Gene names

Name:	ANB1
Synonyms:	HYP1, TIF51B
Ordered Locus Names:	YJR047C
ORF Names:	J1651

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell By similarity. Ref.10 Ref.16 Ref.19 Ref.20
Subunit structure	Homodimer By similarity. Interacts with DYS1 and LIA1 By similarity.
Subcellular location	Cytoplasm. Note: Concentrates in the perinuclear region.
Induction	Expressed in anaerobic conditions. Down-regulated by heme and the ROX1 and REO1 transcription factors in aerobic conditions. Ref.8 Ref.11 Ref.13 Ref.14 Ref.15
Post-translational modification	eIF-5A seems to be the only eukaryotic protein to have an hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).
Miscellaneous	There are two genes for eIF-5A in yeast. Present with 14200 molecules/cell in log phase SD medium. Ref.17
Sequence similarities	Belongs to the eIF-5A family.
Caution	Was originally thought (Ref.10) to be a translation initiation factor but further analysis (Ref.20 and Ref.19) clearly suggests that it is involved in translation elongation and not translation initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Elongation factor
PTM	Acetylation Hypusine Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-lysine modification to hypusine Inferred from electronic annotation. Source: InterPro positive regulation of translational elongation Inferred from electronic annotation. Source: InterPro positive regulation of translational termination Inferred from electronic annotation. Source: InterPro translational frameshifting Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ribosome binding Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 157	156	Eukaryotic translation initiation factor 5A-2		PRO_0000142487
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	51	1	Hypusine
	Modified residue	74	1	Phosphoserine Ref.18

Sequences

	Sequence		Length	Mass (Da)
	P19211 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A578164B760ED9E7	FASTA	157	17,131
	10 20 30 40 50 60 MSDEEHTFEN ADAGASATYP MQCSALRKNG FVVIKGRPCK IVDMSTSKTG KHGHAKVHLV 70 80 90 100 110 120 TLDIFTGKKL EDLSPSTHNL EVPFVKRSEY QLLDIDDGYL SLMTMDGETK DDVKAPEGEL 130 140 150 GDSMQAAFDE GKDLMVTIIS AMGEEAAISF KEAPRSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ANB1 locus of Saccharomyces cerevisiae encodes the protein synthesis initiation factor eIF-4D." Mehta K.D., Leung D., Lefebvre L., Smith M. J. Biol. Chem. 265:8802-8807(1990) [PubMed: 2187871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae." Schnier J., Schwelberger H.G., Smit-Mcbride Z., Kang H.A., Hershey J.W.B. Mol. Cell. Biol. 11:3105-3114(1991) [PubMed: 1903841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Sandholzer U.R. Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DBY874.
[4]	"Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA genes and 14 new open reading frames including a gene most probably belonging to the family of ubiquitin-protein ligases." Huang M.-E., Chuat J.-C., Galibert F. Yeast 11:775-781(1995) [PubMed: 7668047] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[8]	"Identification of an upstream repressor site controlling the expression of an anaerobic gene (ANB1) in Saccharomyces cerevisiae." Mehta K.D., Smith M. J. Biol. Chem. 264:8670-8675(1989) [PubMed: 2656688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, INDUCTION.
[9]	"A hypoxic consensus operator and a constitutive activation region regulate the ANB1 gene of Saccharomyces cerevisiae." Lowry C.V., Esperanza Cerdan M., Zitomer R.S. Mol. Cell. Biol. 10:5921-5926(1990) [PubMed: 2233724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[10]	"The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes." Benne R., Hershey J.W.B. J. Biol. Chem. 253:3078-3087(1978) [PubMed: 641056] [Abstract] Cited for: FUNCTION.
[11]	"Negative regulation of the Saccharomyces cerevisiae ANB1 gene by heme, as mediated by the ROX1 gene product." Lowry C.V., Lieber R.H. Mol. Cell. Biol. 6:4145-4148(1986) [PubMed: 3540607] [Abstract] Cited for: INDUCTION.
[12]	"Hypusine formation in eukaryotic initiation factor 4D is not reversed when rates or specificity of protein synthesis is altered." Gordon E.D., Mora R., Meredith S.C., Lindquist S.L. J. Biol. Chem. 262:16590-16595(1987) [PubMed: 3119589] [Abstract] Cited for: HYPUSINE FORMATION.
[13]	"Identification of REO1, a gene involved in negative regulation of COX5b and ANB1 in aerobically grown Saccharomyces cerevisiae." Trueblood C.E., Poyton R.O. Genetics 120:671-680(1988) [PubMed: 2852136] [Abstract] Cited for: INDUCTION.
[14]	"ROX1 encodes a heme-induced repression factor regulating ANB1 and CYC7 of Saccharomyces cerevisiae." Lowry C.V., Zitomer R.S. Mol. Cell. Biol. 8:4651-4658(1988) [PubMed: 3062365] [Abstract] Cited for: INDUCTION.
[15]	"Translation initiation factor eIF-5A expressed from either of two yeast genes or from human cDNA. Functional identity under aerobic and anaerobic conditions." Schwelberger H.G., Kang H.A., Hershey J.W.B. J. Biol. Chem. 268:14018-14025(1993) [PubMed: 8314769] [Abstract] Cited for: INDUCTION.
[16]	"Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae." Kang H.A., Hershey J.W.B. J. Biol. Chem. 269:3934-3940(1994) [PubMed: 8307948] [Abstract] Cited for: FUNCTION.
[17]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY.
[19]	"eIF5A has a function in the elongation step of translation in yeast." Gregio A.P.B., Cano V.P.S., Avaca J.S., Valentini S.R., Zanelli C.F. Biochem. Biophys. Res. Commun. 380:785-790(2009) [PubMed: 19338753] [Abstract] Cited for: FUNCTION.
[20]	"Hypusine-containing protein eIF5A promotes translation elongation." Saini P., Eyler D.E., Green R., Dever T.E. Nature 459:118-121(2009) [PubMed: 19424157] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05455 Genomic DNA. Translation: AAA34425.1. M63542 Genomic DNA. Translation: AAA35156.1. M60477 Genomic DNA. Translation: AAA34424.1. L36344 Genomic DNA. Translation: AAA88750.1. Z49547 Genomic DNA. Translation: CAA89575.1. AY557894 Genomic DNA. Translation: AAS56220.1. X56235 Genomic DNA. Translation: CAA39692.1. BK006943 Genomic DNA. Translation: DAA08834.1.
PIR	FIBYA2. B40259.
RefSeq	NP_012581.1. NM_001181705.1.
3D structure databases
ProteinModelPortal	P19211.
SMR	P19211. Positions 12-157.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19211. 3 interactions.
MINT	MINT-2788662.
STRING	P19211.
Proteomic databases
PeptideAtlas	P19211.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJR047C; YJR047C; YJR047C.
GeneID	853506.
KEGG	sce:YJR047C.
NMPDR	fig|4932.3.peg.3555.
Organism-specific databases
SGD	S000003808. ANB1.
Phylogenomic databases
eggNOG	fuNOG08157.
GeneTree	EFGT00050000003235.
HOGENOM	HBG526951.
OMA	ICAVKEV.
OrthoDB	EOG4B01ZQ.
Gene expression databases
ArrayExpress	P19211.
Genevestigator	P19211.
GermOnline	YJR047C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005824. KOW. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR019769. Trans_elong_IF5A_hypusine_site. IPR001884. Transl_elong_IF5A. IPR020189. Transl_elong_IF5A_C. IPR014722. Transl_SH3-like_sub. IPR008991. Translation_prot_SH3-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:2.30.30.30. Ribosomal_L2. 1 hit.
KO	K03263.
PANTHER	PTHR11673. EIF5A_hypusine. 1 hit.
Pfam	PF01287. eIF-5a. 1 hit. PF00467. KOW. 1 hit. [Graphical view]
PIRSF	PIRSF003025. eIF5A. 1 hit.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF50104. Transl_SH3_like. 1 hit.
TIGRFAMs	TIGR00037. EIF_5A. 1 hit.
PROSITE	PS00302. IF5A_HYPUSINE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974159.

Entry information

Entry name

IF5A2_YEAST

Accession

Primary (citable) accession number: P19211
Secondary accession number(s): D6VWL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program